Journal article
Structure of three tandem filamin domains reveals auto-inhibition of ligand binding
- Abstract:
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Human filamins are large actin-crosslinking proteins composed of an N-terminal actin-binding domain followed by 24 Ig-like domains (IfFLNs), which interact with numerous transmembrane receptors and cytosolic signaling proteins. Here we report the 2.5 Å resolution structure of a three-domain fragment of human filamin A (IgFLNa19-21). The structure reveals an unexpected domain arrangemetn, with IgFLNa20 partially unfolded bringing IgFLNa21 into close proximity to IgFLNa19. Notably the N-terminu...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Version of record, pdf, 445.5KB, Terms of use)
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(Preview, Version of record, pdf, 1.7MB, Terms of use)
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- Publisher copy:
- 10.1038/sj.emboj.7601827
Authors
Contributors
+ European Molecular Biology Organization
Institution:
University of Oxford
Role:
Other
Funding
+ National Institutes of Health
More from this funder
Funding agency for:
Calderwood, D
Grant:
ROI GM068600-01
Bibliographic Details
- Publisher:
- Nature Publishing Group
- Journal:
- EMBO Journal More from this journal
- Volume:
- 26
- Issue:
- 17
- Pages:
- 3993-4004
- Publication date:
- 2007-09-01
- DOI:
- ISSN:
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1460-2075
Item Description
- Language:
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English
- Keywords:
- Subjects:
- UUID:
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uuid:593888b0-7bdb-4588-a3df-8acc77db2121
- Local pid:
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ora:3162
- Deposit date:
-
2009-12-15
Terms of use
- Copyright holder:
- European Molecular Biology Organization
- Copyright date:
- 2007
- Notes:
- Citation: Lad, Y. et al. (2007). 'Structure of three tandem filamin domains reveals auto-inhibition of ligand binding', The EMBO Journal, 26(17), 3993-4004. [Available at http://www.nature.com/emboj/index.html]. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits distribution, and reproduction in any medium, provided the original author and source are credited. This license does not permit commercial exploitation or the creation of derivative works without specific permission.
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